| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-241629,
cpath:CPATH-LOCAL-241629,
cpath:CPATH-LOCAL-241629,
cpath:CPATH-LOCAL-241630,
cpath:CPATH-LOCAL-241630,
cpath:CPATH-LOCAL-241630,
cpath:CPATH-LOCAL-241631,
cpath:CPATH-LOCAL-241631,
cpath:CPATH-LOCAL-241631,
cpath:CPATH-LOCAL-241632,
cpath:CPATH-LOCAL-241632,
cpath:CPATH-LOCAL-241632,
cpath:CPATH-LOCAL-241633,
cpath:CPATH-LOCAL-241633,
cpath:CPATH-LOCAL-241633,
cpath:CPATH-LOCAL-241634,
cpath:CPATH-LOCAL-241634,
cpath:CPATH-LOCAL-241634,
cpath:CPATH-LOCAL-242682,
cpath:CPATH-LOCAL-242682,
cpath:CPATH-LOCAL-242682
|
| http://www.biopax.org/relea... |
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
|
| http://www.biopax.org/relea... |
PIN1_HUMAN,
PIN1_HUMAN,
PIN1_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
5.2.1.8,
5.2.1.8,
5.2.1.8,
PPIase Pin1,
PPIase Pin1,
PPIase Pin1,
Peptidyl-prolyl cis-trans isomerase Pin1,
Peptidyl-prolyl cis-trans isomerase Pin1,
Peptidyl-prolyl cis-trans isomerase Pin1,
Rotamase Pin1,
Rotamase Pin1,
Rotamase Pin1
|
| http://www.biopax.org/relea... |
FUNCTION: Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzing pSer/Thr-Pro cis/trans isomerizations. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). SUBUNIT: Interacts with STIL (By similarity). Interacts with KIF20B. Interacts with NEK6. SUBCELLULAR LOCATION: Nucleus. Note=Co-localizes with NEK6 in the nucleus. DOMAIN: The WW domain is required for the interaction with STIL and KIF20B. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Contains 1 PpiC domain. SIMILARITY: Contains 1 WW domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzing pSer/Thr-Pro cis/trans isomerizations. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). SUBUNIT: Interacts with STIL (By similarity). Interacts with KIF20B. Interacts with NEK6. SUBCELLULAR LOCATION: Nucleus. Note=Co-localizes with NEK6 in the nucleus. DOMAIN: The WW domain is required for the interaction with STIL and KIF20B. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Contains 1 PpiC domain. SIMILARITY: Contains 1 WW domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzing pSer/Thr-Pro cis/trans isomerizations. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). SUBUNIT: Interacts with STIL (By similarity). Interacts with KIF20B. Interacts with NEK6. SUBCELLULAR LOCATION: Nucleus. Note=Co-localizes with NEK6 in the nucleus. DOMAIN: The WW domain is required for the interaction with STIL and KIF20B. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Contains 1 PpiC domain. SIMILARITY: Contains 1 WW domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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| skos:exactMatch | |
| skos:closeMatch |